RSBRB_BACSU
ID RSBRB_BACSU Reviewed; 277 AA.
AC O34860; Q796M1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=RsbT co-antagonist protein RsbRB;
DE AltName: Full=Stressosome protein RsbRB;
GN Name=rsbRB; Synonyms=ykoB; OrderedLocusNames=BSU13200;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, PHOSPHORYLATION BY RSBT, COMPLEX SUGGESTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=11157946; DOI=10.1128/jb.183.4.1329-1338.2001;
RA Akbar S., Gaidenko T.A., Kang C.M., O'Reilly M., Devine K.M., Price C.W.;
RT "New family of regulators in the environmental signaling pathway which
RT activates the general stress transcription factor sigma(B) of Bacillus
RT subtilis.";
RL J. Bacteriol. 183:1329-1338(2001).
RN [4]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF THR-186 AND THR-220.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=15312768; DOI=10.1016/j.jmb.2004.05.043;
RA Kim T.-J., Gaidenko T.A., Price C.W.;
RT "A multicomponent protein complex mediates environmental stress signaling
RT in Bacillus subtilis.";
RL J. Mol. Biol. 341:135-150(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- FUNCTION: One of 4 functionally non-identical RsbR paralogs, it
CC functions in the environmental signaling branch of the general stress
CC response.
CC -!- FUNCTION: Negative regulator of sigma-B activity. Non-phosphorylated
CC RsbS binds to RsbT, preventing its association with RsbU. Requires any
CC one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and
CC the RsbR paralog(s) are phosphorylated, they release RsbT, which can
CC then bind and activate RsbU.
CC -!- SUBUNIT: Interacts with RsbRA and RsbS in the stressosome. The
CC stressosome probably also contains RsbRC and RsbRD.
CC {ECO:0000269|PubMed:15312768}.
CC -!- PTM: Phosphorylated by RsbT. {ECO:0000269|PubMed:11157946,
CC ECO:0000269|PubMed:17218307}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have an increased sigma-B
CC activity in response to salt and ethanol stress and also increased
CC sigma-B activity in response to the energy stress associated with entry
CC into stationary phase. These results indicate that this protein is a
CC negative regulator of sigma-B activity. {ECO:0000269|PubMed:11157946}.
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DR EMBL; AJ002571; CAA05599.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13177.1; -; Genomic_DNA.
DR PIR; G69646; G69646.
DR RefSeq; NP_389203.1; NC_000964.3.
DR RefSeq; WP_003232560.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34860; -.
DR SMR; O34860; -.
DR STRING; 224308.BSU13200; -.
DR iPTMnet; O34860; -.
DR jPOST; O34860; -.
DR PaxDb; O34860; -.
DR PRIDE; O34860; -.
DR EnsemblBacteria; CAB13177; CAB13177; BSU_13200.
DR GeneID; 938160; -.
DR KEGG; bsu:BSU13200; -.
DR PATRIC; fig|224308.179.peg.1434; -.
DR eggNOG; COG1366; Bacteria.
DR InParanoid; O34860; -.
DR OMA; WYESIED; -.
DR PhylomeDB; O34860; -.
DR BioCyc; BSUB:BSU13200-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR Pfam; PF01740; STAS; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..277
FT /note="RsbT co-antagonist protein RsbRB"
FT /id="PRO_0000361685"
FT DOMAIN 165..276
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MUTAGEN 186
FT /note="T->A: In absence of the other RsbR paralogs
FT decreased stress response."
FT /evidence="ECO:0000269|PubMed:15312768"
FT MUTAGEN 186
FT /note="T->D: In absence of the other RsbR paralogs small
FT decrease in stress response."
FT /evidence="ECO:0000269|PubMed:15312768"
FT MUTAGEN 220
FT /note="T->A: In absence of the other RsbR paralogs no
FT change in stress response."
FT /evidence="ECO:0000269|PubMed:15312768"
FT MUTAGEN 220
FT /note="T->D: In absence of the other RsbR paralogs small
FT decrease in stress response."
FT /evidence="ECO:0000269|PubMed:15312768"
SQ SEQUENCE 277 AA; 32387 MW; F86DD8BD925ACA7D CRC64;
MKLNEKLYAF FSEHVEQMAE EWIETMEESD PNSLYALHNA TVTEELKEQD REFYRHLNYM
YVLPEKQFLE EFQEWVIELT NDQKHLDTPV QYVIREFMRN RRLYTKYFEK FAEENESAFE
PGEKQKWADL IVKVFDFTIY TFVDHAEMNA KQQLNAQREM ILELSSPVIT LSKSTALLPL
VGDIDTERAK FILENTLQAC AKRRVEHLLI DLSGVVVVDT MVAHQIFKLI EALNLIGVRS
TLSGIRPEIA QTAVQLGIDF SNITIKTNLA QALNYHQ
